Phospholipid headgroups govern area per lipid and emergent elastic properties of bilayers

Molugu, Trivikram R.; Thurmond, Robin L.; Alam, Todd M.; Trouard, Theodore P.; Brown, Michael F.

doi:10.1016/j.bpj.2022.09.005

Cited by 6 publications

(4 citation statements)

References 109 publications

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“…We further analyzed the arrangement of the two lipid chains of the phospholipid molecules in simple GUVs and the system after the action of the four egg white peptides. The segmental order parameter ( S CD ) described the physical and chemical properties of the membrane structure and was often used to calculate the structural order of acyl chains in lipid bilayers . As shown in Figure , the experimental results showed that the arrangement of both lipid chains of the phospholipid membrane was reduced after the interaction with egg white peptide, indicating an increase in the phospholipid membrane fluidity.…”

Section: Resultsmentioning

confidence: 99%

“…The segmental order parameter (S CD ) described the physical and chemical properties of the membrane structure and was often used to calculate the structural order of acyl chains in lipid bilayers. 67 As shown in Figure 5, the experimental results showed that the arrangement of both lipid chains of the phospholipid membrane was reduced after the interaction with egg white peptide, indicating an increase in the phospholipid membrane fluidity. Comparing the lipid arrangement of Sn-1 and Sn-2 chains, it could be discovered that the effect of egg white peptides on the Sn-2 chain was more visible.…”

Section: Molecular Mechanistic Analysis Of Peptide-membrane Interactionsmentioning

confidence: 89%

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Molecular Interactions Between Egg White Peptides and Giant Unilamellar Vesicle Membranes: Effect of Peptide Localization on Membrane Fluidity

Zhang,

Fu,

et al. 2024

J. Agric. Food Chem.

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Bioactive peptides have been shown to affect cell membrane fluidity, which is an important indicator of the cell membrane structure and function. However, the underlying mechanism of egg white-derived bioactive peptide regulation of cell membrane fluidity has not been elucidated yet. The cell membrane fluidity was investigated by giant unilamellar vesicles in the present study. The results showed that peptides TCNW, ADWAK, ESIINF, VPIEGII, LVEEY, and WKLC connect to membranes through intermolecular interactions, such as hydrogen bonding and regulated membrane fluidity, in a concentration-dependent way. In addition, peptides prefer to localize in the hydrophobic core of the bilayers. This study provides a theoretical basis for analyzing the localization of egg white bioactive peptides in specific cell membrane regions and their influence on the cell membrane fluidity.

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Section: Resultsmentioning

confidence: 99%

Section: Molecular Mechanistic Analysis Of Peptide-membrane Interactionsmentioning

confidence: 89%

Molecular Interactions Between Egg White Peptides and Giant Unilamellar Vesicle Membranes: Effect of Peptide Localization on Membrane Fluidity

Zhang,

Fu,

et al. 2024

J. Agric. Food Chem.

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“…Clearly the versatility and applicability of molecular simulations hinges upon the robust validation of the trajectories against increasingly stringent experimental data (2,15,(36)(37)(38). Studies related to membrane structure and dynamics rely heavily on the accurate parameterization of the interatomic and intermolecular interactions (28,(39)(40)(41).…”

Section: Introductionmentioning

confidence: 99%

“…The versatility of MD simulations in addressing biophysical questions hinges upon the robust validation of the simulation trajectories against increasingly stringent experimental data (2,12,27). In particular, studies related to membrane structure and dynamics rely heavily on the accurate parameterization of the physics-based interatomic interactions (20,(28)(29)(30).…”

Section: Introductionmentioning

confidence: 99%

Efficient calculation of orientation-dependent lipid dynamics from membrane simulations

Doktorova

Khelashvili

Brown

2023

Preprint

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Molecular dynamics (MD) simulations have become increasingly impactful in membrane biophysics because they offer atomistic resolution into the atomistic fluctuations of lipid assemblies. Validation of the simulation trajectories with experimental data is crucial for interpretation and application of MD results. As an ideal benchmarking technique, NMR spectroscopy delivers order parameters of the carbon-deuterium bond fluctuations along the lipid chains. Additionally, NMR relaxation can access lipid dynamics providing yet another point for validation of simulation force fields. Here we performed short resampling simulations of membrane trajectories to investigate the lipid CH bond fluctuations on sub-40-ps timescales to explore the local fast dynamics. We recently established a robust framework for analysis of NMR relaxation rates from MD simulations, which improves upon current approaches and shows excellent agreement of experimental and theoretical results. The calculation of relaxation rates from simulations presents a universal challenge that we addressed by hypothesizing the existence of fast CH bond dynamics that evade the analysis of simulation data with temporal resolution of 40 ps (or lower). Indeed, our results support this hypothesis confirming the validity of our solution to the sampling problem. Furthermore, we show that the fast CH bond dynamics occur on timescales at which carbon-carbon bond conformations appear nearly stationary and unaffected by cholesterol. Lastly, we discuss the correspondence to the CH bond dynamics of liquid hydrocarbons and relate their existence to the apparent microviscosity of the bilayer hydrocarbon core.

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The role of hydrophobic patches of de novo designed MSI-78 and VG16KRKP antimicrobial peptides on fragmenting model bilayer membranes

Won

Mohid

Choi

et al. 2023

Biophysical Chemistry

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Phospholipid headgroups govern area per lipid and emergent elastic properties of bilayers

Cited by 6 publications

References 109 publications

Molecular Interactions Between Egg White Peptides and Giant Unilamellar Vesicle Membranes: Effect of Peptide Localization on Membrane Fluidity

Molecular Interactions Between Egg White Peptides and Giant Unilamellar Vesicle Membranes: Effect of Peptide Localization on Membrane Fluidity

Efficient calculation of orientation-dependent lipid dynamics from membrane simulations

The role of hydrophobic patches of de novo designed MSI-78 and VG16KRKP antimicrobial peptides on fragmenting model bilayer membranes

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